Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P14922 (CYC8_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
General transcriptional corepressor CYC8
Alternative name(s):
Glucose repression mediator protein CYC8
Gene names
Name:CYC8
Synonyms:CRT8, SSN6
Ordered Locus Names:YBR112C
ORF Names:YBR0908
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length966 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex. Ref.11 Ref.12 Ref.14 Ref.18 Ref.19

Subunit structure

Associates with TUP1 to form the CYC8-TUP1 (or TUP1-SSN6) corepressor complex that is composed of 4 copies of TUP1 and one copy of CYC8. Interacts with MATALPHA2, CTI6, MIG1, TUP1, SUT1, RFX1, PGD1, HOS1, HOS2 AND RPD3. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17

Subcellular location

Nucleus.

Domain

The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form By similarity. Ref.6

Miscellaneous

[OCT+] is the prion form of CYC8. [OCT+] is the result of a conformational change of the cellular CYC8 protein that becomes self-propagating and infectious. [OCT+] aggregates sequester soluble CYC8, resulting in increased levels of iso-2-cytochrome c, defects in sporulation and mating, higher levels of invertase derepression and increased flocculation, reminiscent of a partial loss of function of the CYC8-TUP1 corepressor complex. [OCT+] can be cured by GdnHCl and by inactivation of the molecular chaperone HSP104, which is required for [OCT+] propagation. It is speculated that prion properties of transcription factors may generate an optimized phenotypic heterogeneity that buffers yeast populations against diverse environmental insults (Ref.24).

Present with 3890 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the CYC8/SSN6 family.

Contains 10 TPR repeats.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentAmyloid
Nucleus
   DomainRepeat
TPR repeat
   Molecular functionPrion
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin remodeling

Inferred from genetic interaction PubMed 14739928. Source: SGD

negative regulation of dipeptide transport by negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 18708352. Source: SGD

negative regulation of transcription from RNA polymerase II promoter during mitosis

Inferred from mutant phenotype PubMed 9560430. Source: SGD

nucleosome positioning

Inferred from direct assay PubMed 15116071. Source: SGD

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 9867831. Source: GOC

regulation of fatty acid biosynthetic process by regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 9280286. Source: SGD

regulation of response to DNA damage stimulus

Inferred from mutant phenotype Ref.10. Source: SGD

regulation of transcription from RNA polymerase II promoter in response to osmotic stress

Inferred from mutant phenotype PubMed 9858577. Source: SGD

   Cellular_componentnucleus

Inferred from direct assay PubMed 1739976. Source: SGD

transcriptional repressor complex

Inferred from direct assay PubMed 9111019. Source: SGD

   Molecular_functionRNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay Ref.10. Source: SGD

RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 9867831. Source: SGD

histone deacetylase binding

Inferred from direct assay Ref.17. Source: SGD

protein binding

Inferred from physical interaction Ref.12Ref.11Ref.17PubMed 16429126PubMed 18467557Ref.10. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 966966General transcriptional corepressor CYC8
PRO_0000106327

Regions

Repeat46 – 7934TPR 1
Repeat80 – 11334TPR 2
Repeat114 – 14734TPR 3
Repeat150 – 18334TPR 4
Repeat187 – 22034TPR 5
Repeat224 – 25734TPR 6
Repeat262 – 29534TPR 7
Repeat296 – 32934TPR 8
Repeat330 – 36334TPR 9
Repeat364 – 39835TPR 10
Region467 – 682216Prion domain (PrD)
Compositional bias15 – 3016Poly-Gln

Amino acid modifications

Modified residue4291Phosphoserine Ref.23 Ref.25
Modified residue4751Phosphothreonine Ref.23
Modified residue7101Phosphoserine Ref.22
Modified residue7411Phosphoserine Ref.25
Modified residue7681Phosphoserine Ref.23
Modified residue8151Phosphoserine Ref.21 Ref.25
Modified residue8171Phosphoserine Ref.21 Ref.25
Modified residue8661Phosphoserine Ref.23
Modified residue9431Phosphoserine Ref.21 Ref.23 Ref.25

Experimental info

Sequence conflict5471Q → K in AAA34545. Ref.1
Sequence conflict5471Q → K in AAA35103. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P14922 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: FC2D0D0C1B181207

FASTA966107,202
        10         20         30         40         50         60 
MNPGGEQTIM EQPAQQQQQQ QQQQQQQQQQ AAVPQQPLDP LTQSTAETWL SIASLAETLG 

        70         80         90        100        110        120 
DGDRAAMAYD ATLQFNPSSA KALTSLAHLY RSRDMFQRAA ELYERALLVN PELSDVWATL 

       130        140        150        160        170        180 
GHCYLMLDDL QRAYNAYQQA LYHLSNPNVP KLWHGIGILY DRYGSLDYAE EAFAKVLELD 

       190        200        210        220        230        240 
PHFEKANEIY FRLGIIYKHQ GKWSQALECF RYILPQPPAP LQEWDIWFQL GSVLESMGEW 

       250        260        270        280        290        300 
QGAKEAYEHV LAQNQHHAKV LQQLGCLYGM SNVQFYDPQK ALDYLLKSLE ADPSDATTWY 

       310        320        330        340        350        360 
HLGRVHMIRT DYTAAYDAFQ QAVNRDSRNP IFWCSIGVLY YQISQYRDAL DAYTRAIRLN 

       370        380        390        400        410        420 
PYISEVWYDL GTLYETCNNQ LSDALDAYKQ AARLDVNNVH IRERLEALTK QLENPGNINK 

       430        440        450        460        470        480 
SNGAPTNASP APPPVILQPT LQPNDQGNPL NTRISAQSAN ATASMVQQQH PAQQTPINSS 

       490        500        510        520        530        540 
ATMYSNGASP QLQAQAQAQA QAQAQAQAQA QAQAQAQAQA QAQAQAQAQA QAQAQAHAQA 

       550        560        570        580        590        600 
QAQAQAQAQA QAQAQAQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQLQP LPRQQLQQKG 

       610        620        630        640        650        660 
VSVQMLNPQQ GQPYITQPTV IQAHQLQPFS TQAMEHPQSS QLPPQQQQLQ SVQHPQQLQG 

       670        680        690        700        710        720 
QPQAQAPQPL IQHNVEQNVL PQKRYMEGAI HTLVDAAVSS STHTENNTKS PRQPTHAIPT 

       730        740        750        760        770        780 
QAPATGITNA EPQVKKQKLN SPNSNINKLV NTATSIEENA KSEVSNQSPA VVESNTNNTS 

       790        800        810        820        830        840 
QEEKPVKANS IPSVIGAQEP PQEASPAEEA TKAASVSPST KPLNTEPESS SVQPTVSSES 

       850        860        870        880        890        900 
STTKANDQST AETIELSTAT VPAEASPVED EVRQHSKEEN GTTEASAPST EEAEPAASRD 

       910        920        930        940        950        960 
AEKQQDETAA TTITVIKPTL ETMETVKEEA KMREEEQTSQ EKSPQENTLP RENVVRQVEE 


DENYDD 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the CYC8 gene mediating glucose repression in yeast."
Trumbly R.J.
Gene 73:97-111(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Molecular analysis of SSN6, a gene functionally related to the SNF1 protein kinase of Saccharomyces cerevisiae."
Schultz J., Carlson M.
Mol. Cell. Biol. 7:3637-3645(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Molecular analysis of yeast chromosome II between CMD1 and LYS2: the excision repair gene RAD16 located in this region belongs to a novel group of double-finger proteins."
Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.
Yeast 8:397-408(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis."
Sikorski R.S., Boguski M.S., Goebl M., Hieter P.A.
Cell 60:307-317(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAINS TPR REPEATS.
[7]"The tetratricopeptide repeats of Ssn6 interact with the homeo domain of alpha 2."
Smith R.L., Redd M.J., Johnson A.D.
Genes Dev. 9:2903-2910(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MATALPHA2.
[8]"Repression by SSN6-TUP1 is directed by MIG1, a repressor/activator protein."
Treitel M.A., Carlson M.
Proc. Natl. Acad. Sci. U.S.A. 92:3132-3136(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MIG1.
[9]"The Cyc8 (Ssn6)-Tup1 corepressor complex is composed of one Cyc8 and four Tup1 subunits."
Varanasi U.S., Klis M., Mikesell P.B., Trumbly R.J.
Mol. Cell. Biol. 16:6707-6714(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[10]"The DNA replication and damage checkpoint pathways induce transcription by inhibition of the Crt1 repressor."
Huang M., Zhou Z., Elledge S.J.
Cell 94:595-605(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RFX1.
[11]"Ssn6-Tup1 interacts with class I histone deacetylases required for repression."
Watson A.D., Edmondson D.G., Bone J.R., Mukai Y., Yu Y., Du W., Stillman D.J., Roth S.Y.
Genes Dev. 14:2737-2744(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TUP1; HOS2 AND RPD3, FUNCTION OF THE CYC8-TUP1 COMPLEX.
[12]"Hrs1/Med3 is a Cyc8-Tup1 corepressor target in the RNA polymerase II holoenzyme."
Papamichos-Chronakis M., Conlan R.S., Gounalaki N., Copf T., Tzamarias D.
J. Biol. Chem. 275:8397-8403(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PGD1, FUNCTION OF THE CYC8-TUP1 COMPLEX.
[13]"A sequence resembling a peroxisomal targeting sequence directs the interaction between the tetratricopeptide repeats of Ssn6 and the homeodomain of alpha 2."
Smith R.L., Johnson A.D.
Proc. Natl. Acad. Sci. U.S.A. 97:3901-3906(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MATALPHA2.
[14]"Regulation of the Sko1 transcriptional repressor by the Hog1 MAP kinase in response to osmotic stress."
Proft M., Pascual-Ahuir A., de Nadal E., Arino J., Serrano R., Posas F.
EMBO J. 20:1123-1133(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE CYC8-TUP1 COMPLEX.
[15]"SUT1p interaction with Cyc8p(Ssn6p) relieves hypoxic genes from Cyc8p-Tup1p repression in Saccharomyces cerevisiae."
Regnacq M., Alimardani P., El Moudni B., Berges T.
Mol. Microbiol. 40:1085-1096(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUT1.
[16]"Cti6, a PHD domain protein, bridges the Cyc8-Tup1 corepressor and the SAGA coactivator to overcome repression at GAL1."
Papamichos-Chronakis M., Petrakis T., Ktistaki E., Topalidou I., Tzamarias D.
Mol. Cell 9:1297-1305(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTI6.
[17]"Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo."
Davie J.K., Edmondson D.G., Coco C.B., Dent S.Y.
J. Biol. Chem. 278:50158-50162(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HOS1; HOS2 AND RPD3.
[18]"Histone-dependent association of Tup1-Ssn6 with repressed genes in vivo."
Davie J.K., Trumbly R.J., Dent S.Y.
Mol. Cell. Biol. 22:693-703(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE CYC8-TUP1 COREPRESSOR COMPLEX.
[19]"Recruitment of Tup1-Ssn6 by yeast hypoxic genes and chromatin-independent exclusion of TATA binding protein."
Mennella T.A., Klinkenberg L.G., Zitomer R.S.
Eukaryot. Cell 2:1288-1303(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE CYC8-TUP1 COMPLEX.
[20]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[21]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815; SER-817 AND SER-943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[22]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; THR-475; SER-768; SER-866 AND SER-943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion."
Patel B.K., Gavin-Smyth J., Liebman S.W.
Nat. Cell Biol. 11:344-349(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PRION FORMATION.
[25]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; SER-741; SER-815; SER-817 AND SER-943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23440 Genomic DNA. Translation: AAA34545.1.
M17826 Genomic DNA. Translation: AAA35103.1.
X66247 Genomic DNA. Translation: CAA46973.1.
X78993 Genomic DNA. Translation: CAA55615.1.
Z35981 Genomic DNA. Translation: CAA85069.1.
BK006936 Genomic DNA. Translation: DAA07232.1.
PIRS25365.
RefSeqNP_009670.3. NM_001178460.3.

3D structure databases

ProteinModelPortalP14922.
SMRP14922. Positions 45-395.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32816. 101 interactions.
DIPDIP-696N.
IntActP14922. 10 interactions.
MINTMINT-579675.
STRING4932.YBR112C.

Proteomic databases

MaxQBP14922.
PaxDbP14922.
PeptideAtlasP14922.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR112C; YBR112C; YBR112C.
GeneID852410.
KEGGsce:YBR112C.

Organism-specific databases

SGDS000000316. CYC8.

Phylogenomic databases

eggNOGCOG0457.
GeneTreeENSGT00410000025758.
KOK06665.
OrthoDBEOG7NKKW1.

Enzyme and pathway databases

BioCycYEAST:G3O-29073-MONOMER.

Gene expression databases

GenevestigatorP14922.

Family and domain databases

Gene3D1.25.40.10. 2 hits.
InterProIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF00515. TPR_1. 6 hits.
[Graphical view]
SMARTSM00028. TPR. 10 hits.
[Graphical view]
PROSITEPS50005. TPR. 9 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971258.

Entry information

Entry nameCYC8_YEAST
AccessionPrimary (citable) accession number: P14922
Secondary accession number(s): D6VQB2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families